THE ROLE OF ATP HYDROLYSIS IN THE FUNCTION OF THE CHAPERONIN GROEL - DYNAMIC COMPLEX-FORMATION WITH GROES

被引：11

作者：

KAWATA, Y

HONGO, K

NOSAKA, K

FURUTSU, Y

MIZOBATA, T

NAGAI, J

机构：

[1] Department of Biotechnology, Faculty of Engineering, Tottori University, Tottori

来源：

FEBS LETTERS | 1995年 / 369卷 / 2-3期

关键词：

CHAPERONIN; GROEL-GROES COMPLEX FORMATION; ATP HYDROLYSIS; CAPILLARY ELECTROPHORESIS; SURFACE PLASMON RESONANCE;

D O I：

10.1016/0014-5793(95)00768-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In order to understand the role of ATP hydrolysis of the chaperonin GroEL during protein folding, we have studied GroEL-GroES complex formation in the presence of ATP or ADP by using capillary electrophoresis and surface plasmon resonance. Capillary electrophoresis analysis showed that the GroEL 14-mer and GroES 7-mer formed a 1:1 complex in the presence of ATP. In the presence of ADP, both the association and dissociation rates of the complex were slower by about one order of magnitude than the rates in the presence of ATP at 25 degrees C. The implications of such a stable complex on the overall mechanism of chaperonin function are discussed.

引用

页码：283 / 286

页数：4

共 30 条

[1] BINDING OF A CHAPERONIN TO THE FOLDING INTERMEDIATES OF LACTATE-DEHYDROGENASE [J].